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Merck
CN

525145

sPLA2-IIA Inhibitor I

The sPLA2-IIA Inhibitor I controls the biological activity of sPLA2-IIA. This small molecule/inhibitor is primarily used for Cell Signaling applications.

别名:

sPLA2-IIA Inhibitor I, c(2NapA)LS(2NapA)R, TFA

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关于此项目

经验公式(希尔记法):
C41H50N8O6 · xC2HF3O2
分子量:
750.89 (free base basis)
NACRES:
NA.77
UNSPSC Code:
41106300
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产品名称

sPLA2-IIA Inhibitor I, The sPLA2-IIA Inhibitor I controls the biological activity of sPLA2-IIA. This small molecule/inhibitor is primarily used for Cell Signaling applications.

assay

≥95% (HPLC)

form

lyophilized solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
desiccated (hygroscopic)

color

white

solubility

DMSO: 5 mg/mL

shipped in

ambient

storage temp.

−20°C

Quality Level

Biochem/physiol Actions

Cell permeable: no
Primary Target
sPLA2-IIA (human type IIA secreted phospholipase A2
Product does not compete with ATP.
Reversible: no
Target IC50: 12.8 µM against sPLA2-IIA (human type IIA secreted phospholipase A2

Disclaimer

Toxicity: Standard Handling (A)

General description

A highly hydrophobic cyclic pentapeptide that selectively binds and acts as a potent inhibitor of sPLA2-IIA (human type IIA secreted phospholipase A2; IC50 = 12.8 μM). Shown to effectively block sPLA2-IIA-induced PGE2 production at 100 nM in human rheumatoid synoviocytes and is non-toxic at doses up to 10 μM. Does not have any significant effect on the activities of porcine sPLA2-IB, Naja naja sPLA2-IB, or Crotalus durissus sPLA2-IIA even at 10 μM concentration.

Other Notes

Church, W.B., et al. 2001. J. Biol. Chem.276, 33156.
cyclic(2-NaphthylAla-Leu-Ser-2-NaphthylAla-Arg)•TFA

Packaging

Packaged under inert gas

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

存储类别

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Julien Pothlichet et al.
Frontiers in immunology, 13, 824746-824746 (2022-04-09)
The origin of the impaired CD4 T-cell response and immunodeficiency of HIV-infected patients is still only partially understood. We recently demonstrated that PLA2G1B phospholipase synergizes with the HIV gp41 envelope protein in HIV viremic plasma to induce large abnormal membrane

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